RSSA2_SCHPO
ID RSSA2_SCHPO Reviewed; 287 AA.
AC Q9P546;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=40S ribosomal protein S0-B {ECO:0000255|HAMAP-Rule:MF_03015};
GN Name=rps002; Synonyms=rps0b, rpsa2; ORFNames=SPAPJ698.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, INTERACTION WITH RPS21, AND DISRUPTION PHENOTYPE.
RX PubMed=14623272; DOI=10.1016/j.bbrc.2003.10.086;
RA Sato M., Kong C.J., Yoshida H., Nakamura T., Wada A., Shimoda C.,
RA Kaneda Y.;
RT "Ribosomal proteins S0 and S21 are involved in the stability of 18S rRNA in
RT fission yeast, Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 311:942-947(2003).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC ribosomal subunit. Required for the processing of the 20S rRNA-
CC precursor to mature 18S rRNA in a late step of the maturation of 40S
CC ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015,
CC ECO:0000269|PubMed:14623272}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (25S, 5.8S and 5S). Interacts with rps21. {ECO:0000255|HAMAP-
CC Rule:MF_03015, ECO:0000269|PubMed:14623272}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015,
CC ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Deficiency of 40S ribosomal subunit formation,
CC this is likely to be caused by insufficient 18S rRNA stability.
CC {ECO:0000269|PubMed:14623272}.
CC -!- MISCELLANEOUS: There are two genes for S0 in S.pombe.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR EMBL; CU329670; CAB92099.1; -; Genomic_DNA.
DR RefSeq; NP_594413.1; NM_001019843.2.
DR AlphaFoldDB; Q9P546; -.
DR SMR; Q9P546; -.
DR BioGRID; 279718; 4.
DR STRING; 4896.SPAPJ698.02c.1; -.
DR iPTMnet; Q9P546; -.
DR MaxQB; Q9P546; -.
DR PaxDb; Q9P546; -.
DR PRIDE; Q9P546; -.
DR EnsemblFungi; SPAPJ698.02c.1; SPAPJ698.02c.1:pep; SPAPJ698.02c.
DR GeneID; 2543293; -.
DR KEGG; spo:SPAPJ698.02c; -.
DR PomBase; SPAPJ698.02c; rps002.
DR VEuPathDB; FungiDB:SPAPJ698.02c; -.
DR eggNOG; KOG0830; Eukaryota.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; Q9P546; -.
DR OMA; WEGDAEW; -.
DR PhylomeDB; Q9P546; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SPO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q9P546; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:PomBase.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:PomBase.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR InterPro; IPR032281; 40S_SA_C.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR027498; Ribosomal_S2_euk.
DR InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR11489; PTHR11489; 1.
DR Pfam; PF16122; 40S_SA_C; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..287
FT /note="40S ribosomal protein S0-B"
FT /id="PRO_0000134369"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 287 AA; 31420 MW; 2D3D13FDA6788C66 CRC64;
MAESIARPSV LNATDDDIKN LLAADSHIGS KNLEVRMENY VWKRRSDGIH IINLGKTWEK
LVLAARVIAT IENPADVCVI SSRPYGHRAV LKFAAHTGAT AIAGRFTPGN FTNYITRTYR
EPRLIIVTDP RADAQAIKEA SFVNIPVIAL CDTDSILNHV DVAIPINNKG YKSIGLAWYL
LAREVLRLRG NISRTTAWEV MPDLYFYRDP EEIEREEEQK AAAAAAAEEE AQLAAQTAAA
EFEVTDSAAG TVDPTILDNA TAGQVGQTTW EGDAEWNITG AAPSEWA
